Hepatocellular Uptake of Bile Acids: Evidence for a Carrier-Mediated Transport System*

2015 ◽  
pp. 101-107
Author(s):  
J. C. Glasinovic ◽  
S. Erlinger ◽  
Micheline Dumont ◽  
M. Duval
Keyword(s):  
Bile Acids ◽  
Transport System ◽  
Carrier Mediated Transport

scholarly journals Hepatocellular Uptake of Bile Acids in the Dog: Evidence for a Common Carrier-Mediated Transport System

1975 ◽  
Vol 69 (4) ◽  
pp. 973-981 ◽  
Author(s):  
J.C. Glasinović ◽  
M. Dumont ◽  
M. Duval ◽  
S. Erlinger
Keyword(s):  
Bile Acids ◽  
Transport System ◽  
Carrier Mediated Transport ◽  
Common Carrier

Uptake of bile acids by perfused rat liver

1976 ◽  
Vol 231 (3) ◽  
pp. 734-742 ◽  
Author(s):  
J Reichen ◽  
G Paumgartner
Keyword(s):  
Bile Acids ◽  
Rat Liver ◽  
Chenodeoxycholic Acid ◽  
Competitive Inhibition ◽  
Compartment Model ◽  
Hepatic Uptake ◽  
Perfused Rat Liver ◽  
Multiple Indicator Dilution ◽  
Rapid Injection ◽  
Carrier Mediated Transport

The uptake of 14C-labeled cholic, taurocholic, and chenodeoxycholic acid by the perfused rat liver was studied to characterize the mechanism responsible for hepatic uptake of bile acids. A rapid-injection multiple indicator-dilution technique and the three-compartment model of Goresky were employed. The kinetics of hepatic uptake of the three bile acids could be described by the Michaelis-Menten equation. The maximal uptake velocities (Vmax) were 24.9 +/- 2.2 (mean +/- SD), 20.8 +/- 1.2, 1.2, and 11.4 +/- 0.9 nmol/s-g liver for cholic, taurocholic, and chenodeoxycholic acid, respectively. The corresponding apparent half-saturation constants (Km) were 526 +/- 125, 258 +/- 43, and 236 +/- 48 nmol/g liver. Competitive inhibition could be demonstrated between cholate and taurocholate as well as between cholate and chenodeoxycholate. Substitution of 94% of the Na+ in the perfusion medium decreased the Vmax and the apparent Km of taurocholate uptake by 68 and 55%, respectively. These findings are consistent with the hypothesis that bile acids are taken up into the hepatocyte by Na+-dependent carrier-mediated transport.

scholarly journals Properties of the canalicular bile acid transport system in rat liver

1987 ◽  
Vol 242 (2) ◽  
pp. 465-469 ◽  
Author(s):  
P J Meier ◽  
A S Meier-Abt ◽  
J L Boyer
Keyword(s):  
Bile Acid ◽  
Substrate Specificity ◽  
Bile Acids ◽  
Rat Liver ◽  
Transport System ◽  
Acid Transport ◽  
Bile Acid Transport ◽  
Canalicular Bile ◽  
Disulphonic Acid ◽  
Bile Acid Carrier

4,4-Di-isothiocyanostilbene-2,2′-disulphonic acid inhibition of taurocholate efflux from canalicular vesicles was used to demonstrate that potential driven and ‘carrier’-mediated canalicular excretion of taurocholate occur via a common, rather than two separate, pathways. This electrogenic canalicular bile acid ‘carrier ’ preferentially transports trihydroxylated and conjugated dihydroxylated bile acids, but not the unphysiological oxo bile acids, and possibly extends its substrate specificity to other amphipathic molecules such as sulphobromophthalein.

A carrier-mediated transport system for benzylpenicillin in isolated hepatocytes

1985 ◽  
Vol 37 (1) ◽  
pp. 55-57 ◽  
Author(s):  
Akir Tsuji ◽  
Tetsuya Terasaki ◽  
Ikumi Tamai ◽  
Emi Nakashima ◽  
Kazuhiro Takanosu
Keyword(s):  
Transport System ◽  
Isolated Hepatocytes ◽  
Carrier Mediated Transport

scholarly journals Effect of carrier-mediated transport system on intestinal fosfomycin absorption in situ and in vivo.

1991 ◽  
Vol 14 (2) ◽  
pp. 82-86 ◽  
Author(s):  
Takayuki ISHIZAWA ◽  
Masahiro HAYASHI ◽  
Shoji AWAZU
Keyword(s):  
Transport System ◽  
Carrier Mediated Transport

Polyamine transport system mediates agmatine transport in mammalian cells

2001 ◽  
Vol 281 (1) ◽  
pp. C329-C334 ◽  
Author(s):  
Joseph Satriano ◽  
Masato Isome ◽  
Robert A. Casero ◽  
Scott C. Thomson ◽  
Roland C. Blantz
Keyword(s):  
Transport System ◽  
Mammalian Cells ◽  
Maximal Velocity ◽  
Human Carcinoma ◽  
Mammalian Cell Lines ◽  
Carrier Mediated Transport ◽  
Polyamine Transport ◽  
Polyamine Content ◽  
Polyamine Transporter ◽  
Nih 3T3

Agmatine is a biogenic amine with the capacity to regulate a number of nonreceptor-mediated functions in mammalian cells, including intracellular polyamine content and nitric oxide generation. We observed avid incorporation of agmatine into several mammalian cell lines and herein characterize agmatine transport in mammalian cells. In transformed NIH/3T3 cells, agmatine uptake is energy dependent with a saturable component indicative of carrier-mediated transport. Transport displays an apparent Michaelis-Menten constant of 2.5 μM and a maximal velocity of 280 pmol · min−1 · mg−1 protein and requires a membrane potential across the plasma membrane for uptake. Competition with polyamines, but not cationic molecules that utilize the y+ system transporter, suppresses agmatine uptake. Altering polyamine transporter activity results in parallel changes in polyamine and agmatine uptake. Furthermore, agmatine uptake is abrogated in a polyamine transport-deficient human carcinoma cell line. These lines of evidence demonstrate that agmatine utilizes, and is dependent on, the polyamine transporter for cellular uptake. The fact that this transport system is associated with proliferation could be of consequence to the antiproliferative effects of agmatine.

Transport of salicylate in proximal tubule (S2 segment) isolated from rabbit kidney

1988 ◽  
Vol 254 (4) ◽  
pp. F554-F561
Author(s):  
L. Schild ◽  
F. Roch-Ramel
Keyword(s):  
Proximal Tubule ◽  
Transport System ◽  
Concentration Gradient ◽  
Bath Temperature ◽  
Rabbit Kidney ◽  
Luminal Membrane ◽  
Carrier Mediated Transport ◽  
Secretory Transport ◽  
Luminal Ph

The secretory and reabsorptive transport of salicylate was studied in the isolated and perfused rabbit proximal tubule (S2 segment). Salicylate secretion (Jb----lsal) fulfilled the criteria for a carrier-mediated transport system: Jb----lsal was saturable, was reversibly inhibited by probenecid, and occurred against a concentration gradient. The Km and Vmax for this secretory transport were 80 microM and 3,200 fmol.min-1.mm-1, respectively. At luminal pH of 7.4 and 6.6, salicylate reabsorption (Jl----bsal) was low (100 fmol.min-1.mm-1). Jl----bsal was stimulated by increasing the bath PCO2 or by removing basolateral HCO3-; Jl----bsal was inhibited by ethoxyzolamide and by SITS in the bath. Our results indicate that salicylate reabsorption depends on H+ secretion, consistent with reabsorption by simple nonionic diffusion. When salicylate was present in the lumen only, Jl----bsal increased after inhibition of the secretory transport by adding ouabain or probenecid in the bath or by lowering the bath temperature. These results are compatible with luminal recycling of salicylate, and suggest the presence of a mediated secretory transporter located at the luminal membrane.

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